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Nature. 2016 Nov 17;539(7629):396-401. doi: 10.1038/nature20152. Epub 2016 Oct 17.

Thermophilic archaea activate butane via alkyl-coenzyme M formation.

Author information

1
Max-Planck Institute for Marine Microbiology, 28359 Bremen, Germany.
2
Alfred Wegener Institute Helmholtz Center for Polar and Marine Research, 27570 Bremerhaven, Germany.
3
MARUM, Center for Marine Environmental Sciences, University Bremen, 28359 Bremen, Germany.
4
Center for Biotechnology, Bielefeld University, 33615 Bielefeld, Germany.
5
Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
6
Helmholtz Centre for Environmental Research - UFZ, 04318 Leipzig, Germany.

Abstract

The anaerobic formation and oxidation of methane involve unique enzymatic mechanisms and cofactors, all of which are believed to be specific for C1-compounds. Here we show that an anaerobic thermophilic enrichment culture composed of dense consortia of archaea and bacteria apparently uses partly similar pathways to oxidize the C4 hydrocarbon butane. The archaea, proposed genus 'Candidatus Syntrophoarchaeum', show the characteristic autofluorescence of methanogens, and contain highly expressed genes encoding enzymes similar to methyl-coenzyme M reductase. We detect butyl-coenzyme M, indicating archaeal butane activation analogous to the first step in anaerobic methane oxidation. In addition, Ca. Syntrophoarchaeum expresses the genes encoding β-oxidation enzymes, carbon monoxide dehydrogenase and reversible C1 methanogenesis enzymes. This allows for the complete oxidation of butane. Reducing equivalents are seemingly channelled to HotSeep-1, a thermophilic sulfate-reducing partner bacterium known from the anaerobic oxidation of methane. Genes encoding 16S rRNA and methyl-coenzyme M reductase similar to those identifying Ca. Syntrophoarchaeum were repeatedly retrieved from marine subsurface sediments, suggesting that the presented activation mechanism is naturally widespread in the anaerobic oxidation of short-chain hydrocarbons.

PMID:
27749816
DOI:
10.1038/nature20152
[Indexed for MEDLINE]

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